Differences in endogenous peptides presented by HLA-B*2705 and B*2703 allelic variants. Implications for susceptibility to spondylarthropathies
about
A peptide filtering relation quantifies MHC class I peptide optimizationImmunoproteomics: Mass spectrometry-based methods to study the targets of the immune responseIdentification of novel HLA-B27 ligands derived from polymorphic regions of its own or other class I molecules based on direct generation by 20 S proteasome.The Cys-67 residue of HLA-B27 influences cell surface stability, peptide specificity, and T-cell antigen presentation.Minimal alterations in the HLA-B27-bound peptide repertoire induced upon infection of lymphoid cells with Salmonella typhimurium.Human Leukocyte Antigen (HLA) B27 Allotype-Specific Binding and Candidate Arthritogenic Peptides Revealed through Heuristic Clustering of Data-independent Acquisition Mass Spectrometry (DIA-MS) Data.Cytotoxic T-cell-mediated response against Yersinia pseudotuberculosis in HLA-B27 transgenic rat.Overlapping peptide-binding specificities of HLA-B27 and B39: evidence for a role of peptide supermotif in the pathogenesis of spondylarthropathies.Human leukocyte antigen typing using a knowledge base coupled with a high-throughput oligonucleotide probe array analysis.A common minimal motif for the ligands of HLA-B*27 class I molecules.Use of proteomics to define targets of T-cell immunity.Molecular mimicry of an HLA-B27-derived ligand of arthritis-linked subtypes with chlamydial proteins.Peptide handling by HLA-B27 subtypes influences their biological behavior, association with ankylosing spondylitis and susceptibility to endoplasmic reticulum aminopeptidase 1 (ERAP1).Functional interaction of the ankylosing spondylitis-associated endoplasmic reticulum aminopeptidase 1 polymorphism and HLA-B27 in vivo.Alteration of HLA-B27 peptide presentation after infection of transfected murine L cells by Shigella flexneri.HLA-B27-restricted T cells from patients with ankylosing spondylitis recognize peptides from B*2705 that are similar to bacteria-derived peptides.Differential association of HLA-B*2705 and B*2709 to ankylosing spondylitis correlates with limited peptide subsets but not with altered cell surface stability.The South Amerindian allotype HLA-B*3909 has the largest known similarity in peptide specificity and common natural ligands with HLA-B27.Purification, crystallization and preliminary X-ray diffraction analysis of the human major histocompatibility antigen HLA-B*2703 complexed with a viral peptide and with a self-peptide.Long-range effects in protein--ligand interactions mediate peptide specificity in the human major histocompatibilty antigen HLA-B27 (B*2701).
P2860
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P2860
Differences in endogenous peptides presented by HLA-B*2705 and B*2703 allelic variants. Implications for susceptibility to spondylarthropathies
description
article científic
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article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1996
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Differences in endogenous pept ...... bility to spondylarthropathies
@en
Differences in endogenous pept ...... ility to spondylarthropathies.
@nl
type
label
Differences in endogenous pept ...... bility to spondylarthropathies
@en
Differences in endogenous pept ...... ility to spondylarthropathies.
@nl
prefLabel
Differences in endogenous pept ...... bility to spondylarthropathies
@en
Differences in endogenous pept ...... ility to spondylarthropathies.
@nl
P2093
P2860
P356
P1476
Differences in endogenous pept ...... bility to spondylarthropathies
@en
P2093
Boisgérault F
Stolzenberg MC
P2860
P304
P356
10.1172/JCI119102
P407
P577
1996-12-01T00:00:00Z